Evidence map›Paper›PMID 12029030›Full record

ArticleJournal of bacteriology2002

Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+).

David G Kehres, Anu Janakiraman, James M Slauch, Michael E Maguire

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
8.1field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

87 citing papers in PubMed, 142 citations in OpenAlex.

  1. Article
  2. Microbes vary strategically in their metalation of mononuclear enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Manganese transporters regulate the resumption of replication in hydrogen peroxide-stressed Escherichia coli.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  8. An Intrinsic Alkalization Circuit Turns onMicrobiology spectrum · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Manganese Utilization inFrontiers in cell and developmental biology · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

David G KehresDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965, USA. dgk2@po.cwru.edu
Anu Janakiraman
James M Slauch
Michael E Maguire
Case Western Reserve University · USUniversity of Illinois Urbana-Champaign · US

Funding

Manganese Homeostasis and SalmonellaR01GM061748 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MAGUIRE, MICHAEL E · 2002 to 2005
$1.1M
NIGMS NIH HHS GM61748NIGMS NIH HHS R01 GM061748
6 · The paper itself

Abstract

MntH, a bacterial homolog of mammalian natural resistance associated macrophage protein 1 (Nramp1), is a primary transporter for Mn(2+) influx in Salmonella enterica serovar Typhimurium and Escherichia coli. S. enterica serovar Typhimurium MntH contributes to H(2)O(2) resistance and is important for full virulence. Consistent with its phenotype and function, mntH is regulated at the transcriptional level by both H(2)O(2) and substrate cation. We have now identified three trans-acting regulatory factors and the three corresponding cis-acting mntH promoter motifs that mediate this regulation. In the presence of hydrogen peroxide, mntH is activated by OxyR, acting through an OxyR-binding motif centered just upstream of the likely -35 RNA polymerase-binding site. In the presence of Fe(2+), mntH is repressed primarily by Fur, acting through a Fur-binding motif overlapping the -35 region. In the presence of Mn(2+), mntH is repressed primarily by the Salmonella equivalent of E. coli b0817, a distant homolog of the Bacillus subtilis manganese transport repressor, MntR, acting through an inverted-repeat motif located between the likely -10 polymerase binding site and the ribosome binding site. E. coli b0817 was recently shown to bind the identical inverted-repeat motif in the E. coli mntH promoter and hence has been renamed MntR (S. I. Patzer and K. Hantke, J. Bacteriol. 183:4806-4813, 2001). Using Deltafur, DeltamntR, and Deltafur DeltamntR mutant strains as well as mutations in the Fur- and MntR-binding motif elements, we found that Fe(2+) can also mediate repression through the Mn(2+) repressor MntR.

Indexed as

Bacterial ProteinsCation Transport ProteinsEscherichia coli ProteinsGene Expression Regulation, BacterialTranscription, GeneticBase SequenceCarrier ProteinsFerrous CompoundsHydrogen PeroxideManganeseMolecular Sequence DataPromoter Regions, GeneticRepressor ProteinsSalmonella typhimuriumBacterial ProteinsCarrier ProteinsCation Transport ProteinsEscherichia coli ProteinsFerrous CompoundsHydrogen PeroxideManganeseMntH protein, bacteriaMntH protein, E coliRepressor Proteins

Identifiers

PMID12029030
PMCPMC135095
OpenAlexW2099910134

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.